{"product_id":"carbohydrate-based-drug-discovery-2-volume-set-9783527306329","title":"Carbohydrate-based Drug Discovery, 2 Volume Set","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003eTo exploit the full potential of this diverse compound class for the development of novel active substances, this handbook presents the latest knowledge on carbohydrate chemistry and biochemistry. While it is unique in covering the entire field, particular emphasis is placed on carbohydrates with pharmaceutical potential.\u003cbr\u003e Topics include the following:\u003cbr\u003e \u0026gt; Chemical Synthesis of Carbohydrates\u003cbr\u003e \u0026gt; Carbohydrate Biosynthesis and Metabolism\u003cbr\u003e \u0026gt; Carbohydrate Analysis\u003cbr\u003e \u0026gt; Cellular Functions of Carbohydrates\u003cbr\u003e \u0026gt; Development of Carbohydrate-based Drugs\u003cbr\u003e A premier resource for carbohydrate chemists and drug developers, this comprehensive two-volume work contains contributions by more than 50 of the world's leading carbohydrate chemists.\u003cbr\u003e\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTrade Review\u003c\/b\u003e\u003cbr\u003e\"In summary, Carbohydrate-Based Drug Discovery Vols. 1 and 2 provide an appropriate and useful look at the current state of the art in this relevant and rapidly advancing field. I recommend the book to both experts and less expert readers.\"\u003cbr\u003e \u003cbr\u003e Francesco Nicotra, Universita di Milano-Bicocca (Italy)\u003cbr\u003e ChemBioChem 4\/2004\u003cbr\u003e \u003cbr\u003e \"To summarize, the work provides a comprehensive and excellent survey of the present situation in carbohydrate research, in which many interesting details can be spotted. Because of the wide range of topics covered, the reader will refer to it again and again. It is likely to become a standard work on the subject, not exclusively for carbohydrate chemistry enthusiasts.\"\u003cbr\u003e \u003cbr\u003e Oliver Plettenburg, Ulrich Stilz\u003cbr\u003e Angewandte Chemie + IE 2004-43\/31\u003cbr\u003e\"Leser mit soliden organisch-chemischen Kenntnissen werden ihre wahre Freude an diesem spannenden Einblick in die moderne Zuckerchemie haben.\"\u003cbr\u003e \u003cbr\u003e BioTec März\/April 2004\u003cbr\u003e \u003cbr\u003e \"Zusammenfassend stellt dieses Werk einerseits eine nahezu unerschöpfliche Quelle für den Chemiker und Forscher\/Entwickler in der Pharmazeutischen Industrie dar. Andererseits zeigt es aber auch dem Mediziner, Pharmazeuten und Naturwissenschaftler neue, innovative Wege und Tendenzen...auf.\"\u003cbr\u003e A. Schmidt\u003cbr\u003e Der Mikrobiologe\u003cbr\u003e \u003cbr\u003e \"Insgesamt ist das vorliegende Werk eine umfassende und sehr gelungene Zusammenstellung des aktuellen Standes der Kohlenhydratforschung, in der es viel zu entdecken gibt. Der Facettenreichtum des diskutierten Stoffes wird den Leser immer wieder zu den beiden Bänden greifen lassen. Nicht nur für Freunde der Zuckerchemie sollte Carbohydrate-based Drug Discovery zu einem Standardwerk werden.\"\u003cbr\u003e \u003cbr\u003e Oliver Plettenburg, Ulrich Stilz\u003cbr\u003e Angewandte Chemie + IE 2004-43\/31\u003cbr\u003e \u003cbr\u003e \u003cbr\u003e \"Professionalität und ein gutes wissenschaftliches Netzwerk zahlen sich für die Qualität eines derartig innovativen Werkes einer noch etwas stiefmütterlich behandelten Richtung der Wissenschaft nachhaltig aus.\"\u003cbr\u003e \u003cbr\u003e A. Schmidt\u003cbr\u003e Arzneimittel-Forschung \/ Drug Research 8\/04\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e\u003cb\u003eVolume 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003ePreface xxv\u003c\/p\u003e \u003cp\u003eList of Contributors xxvii\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Synthetic Methodologies \u003c\/b\u003e\u003cb\u003e1\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eChikako Saotome and Osamu Kanie\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e1.1 Introduction 1\u003c\/p\u003e \u003cp\u003e1.2 Tactical Analysis for Overall Synthetic Efficiency 1\u003c\/p\u003e \u003cp\u003e1.3 Methodological Improvements 2\u003c\/p\u003e \u003cp\u003e1.4 Accessibility 11\u003c\/p\u003e \u003cp\u003e1.5 Concluding Remarks 32\u003c\/p\u003e \u003cp\u003e1.6 References 33\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Complex Carbohydrate Synthesis \u003c\/b\u003e\u003cb\u003e37\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eMakoto Kiso, Hideharu Ishida, and Hiromune Ando\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e2.1 Introduction 37\u003c\/p\u003e \u003cp\u003e2.2 Synthetic Gangliosides 38\u003c\/p\u003e \u003cp\u003e2.3 Toxin Receptor 50\u003c\/p\u003e \u003cp\u003e2.4 Summary and Perspectives 52\u003c\/p\u003e \u003cp\u003e2.5 References 52\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 The Chemistry of Sialic Acid \u003c\/b\u003e\u003cb\u003e55\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eGeert-Jan Boons and Alexei V. Demchenko\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e3.1 Introduction 55\u003c\/p\u003e \u003cp\u003e3.2 Chemical and Enzymatic Synthesis of Sialic Acids 56\u003c\/p\u003e \u003cp\u003e3.3 Chemical Glycosidation of Sialic Acids 59\u003c\/p\u003e \u003cp\u003e3.4 Enzymatic Glycosidations of Sialic Acids 83\u003c\/p\u003e \u003cp\u003e3.5 Synthesis of \u003ci\u003eC\u003c\/i\u003e- and \u003ci\u003eS\u003c\/i\u003e-Glycosides of Sialic Acid 91\u003c\/p\u003e \u003cp\u003e3.6 Modifications at \u003ci\u003eN\u003c\/i\u003e-5 94\u003c\/p\u003e \u003cp\u003e3.7 References 95\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Solid-Phase Oligosaccharide Synthesis \u003c\/b\u003e\u003cb\u003e103\u003cbr\u003e\u003c\/b\u003e\u003ci\u003ePeter H. Seeberger\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e4.1 Introduction 103\u003c\/p\u003e \u003cp\u003e4.2 Pioneering Efforts in Solid-Phase Oligosaccharide Synthesis 104\u003c\/p\u003e \u003cp\u003e4.3 Synthetic Strategies 105\u003c\/p\u003e \u003cp\u003e4.4 Support Materials 107\u003c\/p\u003e \u003cp\u003e4.5 Linkers 108\u003c\/p\u003e \u003cp\u003e4.6 Synthesis of Oligosaccharides on Solid Support by Use of Different Glycosylating Agents 112\u003c\/p\u003e \u003cp\u003e4.7 Automated Solid-Phase Oligosaccharide Synthesis 118\u003c\/p\u003e \u003cp\u003e4.8 Conclusion and Outlook 124\u003c\/p\u003e \u003cp\u003e4.9 References 125\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Solution and Polymer-Supported Synthesis of Carbohydrates \u003c\/b\u003e\u003cb\u003e129\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eShin-Ichiro Nishimura\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e5.1 Introduction 129\u003c\/p\u003e \u003cp\u003e5.2 Mimicking Glycoprotein Biosynthetic Systems 130\u003c\/p\u003e \u003cp\u003e5.3 References 136\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Enzymatic Synthesis of Oligosaccharides\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eJianbo Zhang, Jun Shao, Prezemk Kowal, and Peng George Wang\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e6.1 Introduction 137\u003c\/p\u003e \u003cp\u003e6.2 Sugar Nucleotide Biosynthetic Pathways 140\u003c\/p\u003e \u003cp\u003e6.3 Enzymatic Oligosaccharide Synthesis Processes 151\u003c\/p\u003e \u003cp\u003e6.4 Future Directions 162\u003c\/p\u003e \u003cp\u003e6.5 References 162\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Glycopeptides and Glycoproteins: Synthetic Chemistry and Biology \u003c\/b\u003e\u003cb\u003e169\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eOliver Seitz\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e7.1 Introduction 169\u003c\/p\u003e \u003cp\u003e7.2 The Glycosidic Linkage 169\u003c\/p\u003e \u003cp\u003e7.3 The Challenges of Glycopeptide Synthesis 171\u003c\/p\u003e \u003cp\u003e7.4 Synthesis of Preformed Glycosyl Amino Acids 173\u003c\/p\u003e \u003cp\u003e7.5 Synthesis of Glycopeptides 181\u003c\/p\u003e \u003cp\u003e7.6 Biological and Biophysical Studies 200\u003c\/p\u003e \u003cp\u003e7.7 Summary and Outlook 208\u003c\/p\u003e \u003cp\u003e7.8 References 209\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Synthesis of Complex Carbohydrates: Everninomicin 13,384-1 \u003c\/b\u003e\u003cb\u003e215\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eK. C. Nicolaou, Helen J. Mitchell, and Scott A. Snyder\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e8.1 Introduction 215\u003c\/p\u003e \u003cp\u003e8.2 Retrosynthetic Analysis and Strategy 218\u003c\/p\u003e \u003cp\u003e8.3 Total Synthesis of Everninomicin 13,384-1 (1) 223\u003c\/p\u003e \u003cp\u003e8.4 Conclusion 249\u003c\/p\u003e \u003cp\u003e8.5 References 250\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Chemical Synthesis of Asparagine-Linked Glycoprotein Oligosaccharides: Recent Examples \u003c\/b\u003e\u003cb\u003e253\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eYukishige Ito and Ichiro Matsuo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e9.1 Introduction 253\u003c\/p\u003e \u003cp\u003e9.2 Synthesis of Asn-Linked Oligosaccharides: Basic Principles 257\u003c\/p\u003e \u003cp\u003e9.3 Chemical Synthesis of Complex Oligosaccharides 261\u003c\/p\u003e \u003cp\u003e9.4 References 278\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Chemistry and Biochemistry of Asparagine-Linked Protein Glycosylation \u003c\/b\u003e\u003cb\u003e281\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eBarbara Imperiali and Vincent W.-F. Tai\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e10.1 Protein Glycosylation 281\u003c\/p\u003e \u003cp\u003e10.2 Small-Molecule Probes of the Biochemistry of Oligosaccharyl Transferase 283\u003c\/p\u003e \u003cp\u003e10.3 Conclusions 301\u003c\/p\u003e \u003cp\u003e10.4 References 301\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Conformational Analysis of \u003ci\u003eC\u003c\/i\u003e-Glycosides and Related Compounds: Programming Conformational Profiles of \u003ci\u003eC\u003c\/i\u003e- and \u003ci\u003eO\u003c\/i\u003e-Glycosides \u003c\/b\u003e\u003cb\u003e305\u003cbr\u003e\u003c\/b\u003e\u003ci\u003ePeter G. Goekjian, Alexander Wei, and Yoshito Kishi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e11.1 Introduction 305\u003c\/p\u003e \u003cp\u003e11.2 Stereoelectronic Effects and te \u003ci\u003eexo\u003c\/i\u003e-Anomeric Conformation 306\u003c\/p\u003e \u003cp\u003e11.3 Conformational Analysis of \u003ci\u003eC\u003c\/i\u003e-Glycosides: \u003ci\u003eC\u003c\/i\u003e-Monoglycosides 309\u003c\/p\u003e \u003cp\u003e11.4 1,4-Linked \u003ci\u003eC\u003c\/i\u003e-Disaccharides: the Importance of \u003ci\u003esyn\u003c\/i\u003e-Pentane Interactions 314\u003c\/p\u003e \u003cp\u003e11.5 Prediction of Conformational Preference and Experimental Validation 318\u003c\/p\u003e \u003cp\u003e11.6 Programming Oligosaccharide Conformation 322\u003c\/p\u003e \u003cp\u003e11.7 Conformational Design of \u003ci\u003eC-\u003c\/i\u003eTrisaccharides based on a Human Blood Group Antigen 323\u003c\/p\u003e \u003cp\u003e11.8 Conformational Design: Relationship to Biological Activity 330\u003c\/p\u003e \u003cp\u003e11.9 Concluding Remarks 336\u003c\/p\u003e \u003cp\u003e11.10 Acknowledgements 337\u003c\/p\u003e \u003cp\u003e11.11 References 337\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Synthetic Lipid A Antagonists for Sepsis Treatment \u003c\/b\u003e\u003cb\u003e341\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eWilliam J. Christ, Lynn D. Hawkins, Michael D. Lewis, and Yoshito Kishi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e12.1 Background 341\u003c\/p\u003e \u003cp\u003e12.2 Hypothesis and Approach 342\u003c\/p\u003e \u003cp\u003e12.3 Conclusion 351\u003c\/p\u003e \u003cp\u003e12.4 Acknowledgement 353\u003c\/p\u003e \u003cp\u003e12.5 References 353\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Polysialic Acid Vaccines \u003c\/b\u003e\u003cb\u003e357\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eHarold J. Jennings\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e13.1 Introduction 357\u003c\/p\u003e \u003cp\u003e13.2 Group C Meningococcal Vaccines 358\u003c\/p\u003e \u003cp\u003e13.3 Group B Meningococcal Vaccines 362\u003c\/p\u003e \u003cp\u003e13.4 Chemically Modified Group B Meningococcal Vaccines 366\u003c\/p\u003e \u003cp\u003e13.5 Cancer Vaccines 371\u003c\/p\u003e \u003cp\u003e13.6 Acknowledgements 375\u003c\/p\u003e \u003cp\u003e13.7 References 375\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Synthetic Carbohydrate-Based Vaccines \u003c\/b\u003e\u003cb\u003e381\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eStacy J. Keding and Samuel J. Danishefsky\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e14.1 Introduction 381\u003c\/p\u003e \u003cp\u003e14.2 Cancer Vaccines 382\u003c\/p\u003e \u003cp\u003e14.3 Bacterial Polysaccharide Vaccines 397\u003c\/p\u003e \u003cp\u003e14.4 Synthetic Parasitic Polysaccharide Conjugate Vaccine 402\u003c\/p\u003e \u003cp\u003e14.5 Conclusions 403\u003c\/p\u003e \u003cp\u003e14.6 References 403\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Chemistry, Biochemistry, and Pharmaceutical Potentials of Glycosaminoglycans and Related Saccharides \u003c\/b\u003e\u003cb\u003e407\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eTasneem Islam and Robert J. Linhardt\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e15.1 Introduction 407\u003c\/p\u003e \u003cp\u003e15.2 Dermatan and Chondroitin Sulfates 417\u003c\/p\u003e \u003cp\u003e15.3 Hyaluronan 419\u003c\/p\u003e \u003cp\u003e15.4 Keratan Sulfate 423\u003c\/p\u003e \u003cp\u003e15.5 Other Acidic Polysaccharides 425\u003c\/p\u003e \u003cp\u003e15.6 Pharmaceutical Potential and Challenges 430\u003c\/p\u003e \u003cp\u003e15.7 Conclusion 432\u003c\/p\u003e \u003cp\u003e15.8 References 433\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 A New Generation of Antithrombotics Based on Synthetic Oligosaccharides \u003c\/b\u003e\u003cb\u003e441\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eMaurice Petitou and Jean-Marc Herbert\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e16.1 Introduction 441\u003c\/p\u003e \u003cp\u003e16.2 Heparin and Its Mechanism of Action as an Antithrombotic Agent 442\u003c\/p\u003e \u003cp\u003e16.3 Synthetic Pentasaccharides, Selective Factor Xa Inhibitors, are Antithrombotic Agents 446\u003c\/p\u003e \u003cp\u003e16.4 Synthetic Thrombin-Inhibiting Oligosaccharides: The Next Generation? 452\u003c\/p\u003e \u003cp\u003e16.5 The Mechanism of Antithrombin Activation by Synthetic Oligosaccharides 456\u003c\/p\u003e \u003cp\u003e16.6 Conclusion and Perspectives 456\u003c\/p\u003e \u003cp\u003e16.7 References 457\u003c\/p\u003e \u003cp\u003e\u003cb\u003eVolume 2\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Sequencing of Oligosaccharides and Glycoproteins \u003c\/b\u003e\u003cb\u003e461\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eStuart M. Haslam, Kay-Hooi Khoo, and Anne Dell\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e17.1 Mass Spectrometry 462\u003c\/p\u003e \u003cp\u003e17.2 MS-Based Sequencing Strategies 466\u003c\/p\u003e \u003cp\u003e17.3 Glycan Sequencing and Structural Determination – A Case Study 470\u003c\/p\u003e \u003cp\u003e17.4 Mammalian Glycomics 475\u003c\/p\u003e \u003cp\u003e17.5 Some Special Case Strategies 477\u003c\/p\u003e \u003cp\u003e17.6 References 481\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 Preparation of Heterocyclic 2-Deoxystreptamine Aminoglycoside Analogues and Characterization of their Interaction with RNAs by Use of Electrospray Ionization Mass Spectrometry \u003c\/b\u003e\u003cb\u003e483\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eRichard H. Griffey, Steven A. Hofstadler, and Eric E. Swayze\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e18.1 Introduction 483\u003c\/p\u003e \u003cp\u003e18.2 ESI-MS for Characterization of Aminoglycoside-RNA Interactions 484\u003c\/p\u003e \u003cp\u003e18.3 Preparation of Heterocyclic 2-Deoxystreptamines and Binding to a 16S A Site RNA Model 490\u003c\/p\u003e \u003cp\u003e18.4 Preparation, Binding, and Biological Activity of Substituted Paromomycin Derivatives 495\u003c\/p\u003e \u003cp\u003e18.5 Future Prospects 498\u003c\/p\u003e \u003cp\u003e18.6 Acknowledgements 498\u003c\/p\u003e \u003cp\u003e18.7 References 498\u003c\/p\u003e \u003cp\u003e\u003cb\u003e19 Glycosylation Analysis of a Recombinant P-Selectin Antagonist by High-pH Anion-Exchange Chromatography with Pulsed Electrochemical Detection (HPAEC\/PED) \u003c\/b\u003e\u003cb\u003e501\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eMark R. Hardy and Richard J. Cornell\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e19.1 Introduction 501\u003c\/p\u003e \u003cp\u003e19.2 Use of HPAEC\/PED in the Development of Biopharmaceuticals 502\u003c\/p\u003e \u003cp\u003e19.3 Biology of P-Selectin 503\u003c\/p\u003e \u003cp\u003e19.4 HPAEC\/PED as an Adjunct to rPSGL-Ig Process Development 504\u003c\/p\u003e \u003cp\u003e19.5 Results and Discussion 508\u003c\/p\u003e \u003cp\u003e19.6 Summary 515\u003c\/p\u003e \u003cp\u003e19.7 Acknowledgements 516\u003c\/p\u003e \u003cp\u003e19.8 References 516\u003c\/p\u003e \u003cp\u003e\u003cb\u003e20 Analytical Techniques for the Characterization and Sequencing of Glycosaminoglycans \u003c\/b\u003e\u003cb\u003e517\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eRam Sasisekharan, Zachary Shriver, Mallik Sundaram, and Ganesh Venkataraman\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e20.1 Introduction to GAG Linear Complex Polysaccharides 517\u003c\/p\u003e \u003cp\u003e20.2 Depolymerization of Nascent GAG Chains 521\u003c\/p\u003e \u003cp\u003e20.4 Analytical Tools Used in the Structural Characterization of GAGs 527\u003c\/p\u003e \u003cp\u003e20.5 Future Directions 536\u003c\/p\u003e \u003cp\u003e20.6 Acknowledgements 537\u003c\/p\u003e \u003cp\u003e20.7 References 537\u003c\/p\u003e \u003cp\u003e\u003cb\u003e21 Thermodynamic Models of the Multivalency Effect \u003c\/b\u003e\u003cb\u003e541\u003cbr\u003e\u003c\/b\u003e\u003ci\u003ePavel I. Kitov and David R. Bundle\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e21.1 Introduction 541\u003c\/p\u003e \u003cp\u003e21.2 Concept of Distribution Free Energy 542\u003c\/p\u003e \u003cp\u003e21.3 Multivalent Receptor vs. Monovalent Ligand 546\u003c\/p\u003e \u003cp\u003e21.4 Multivalent Receptor vs. Multivalent Ligand 551\u003c\/p\u003e \u003cp\u003e21.5 Topological Classification of Multivalent Systems 553\u003c\/p\u003e \u003cp\u003e21.6 Determination of Microscopic Binding Parameters by Molecular Modeling 555\u003c\/p\u003e \u003cp\u003e21.7 Determination of Microscopic Binding Parameters from Binding Data 561\u003c\/p\u003e \u003cp\u003e21.8 Thermodynamic Analysis of Multivalent Interaction 562\u003c\/p\u003e \u003cp\u003e21.9 Conclusions 570\u003c\/p\u003e \u003cp\u003e21.10 Mathematical Appendix 570\u003c\/p\u003e \u003cp\u003e21.10.1 Calculation of Statistical Coefficients 570\u003c\/p\u003e \u003cp\u003e21.10.2 Multivalent Receptor and Monovalent Ligand 571\u003c\/p\u003e \u003cp\u003e21.10.3 Multivalent Binding with Linear and Circular Topology 571\u003c\/p\u003e \u003cp\u003e21.10.4 Multivalent Binding with Radial Topology 572\u003c\/p\u003e \u003cp\u003e21.10.5 Derivation of Eq. (24) 572\u003c\/p\u003e \u003cp\u003e21.11 References 573\u003c\/p\u003e \u003cp\u003e\u003cb\u003e22 Synthetic Multivalent Carbohydrate Ligands as Effectors or Inhibitors of Biological Processes \u003c\/b\u003e\u003cb\u003e575\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eLaura L. Kiessling, Jason K. Pontrello, and Michael C. Schuster\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e22.1 Introduction 575\u003c\/p\u003e \u003cp\u003e22.2 Multivalent Carbohydrate Ligands as Inhibitors 581\u003c\/p\u003e \u003cp\u003e22.3 Multivalent Carbohydrate Ligands as Effectors 596\u003c\/p\u003e \u003cp\u003e22.4 Conclusions 605\u003c\/p\u003e \u003cp\u003e22.5 References 605\u003c\/p\u003e \u003cp\u003e\u003cb\u003e23 Glycosyltransferase Inhibitors \u003c\/b\u003e\u003cb\u003e609\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eKarl-Heinz Jung and Richard R. Schmidt\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e23.1 Introduction 609\u003c\/p\u003e \u003cp\u003e23.2 Glycosyltransferases Utilizing NDP-Sugar Donors 610\u003c\/p\u003e \u003cp\u003e23.3 Glycosyltransferases Utilizing NMP-Sugar Donors 641\u003c\/p\u003e \u003cp\u003e23.4 Bisubstrate Analogues as Inhibitors 648\u003c\/p\u003e \u003cp\u003e23.5 Conclusion 653\u003c\/p\u003e \u003cp\u003e23.6 References 654\u003c\/p\u003e \u003cp\u003e\u003cb\u003e24 RNA-Aminoglycoside Interactions \u003c\/b\u003e\u003cb\u003e661\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eHaim Weizman and Yitzhak Tor\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e24.1 RNA as an Emerging Therapeutic Target 661\u003c\/p\u003e \u003cp\u003e24.2 Aminoglycoside Antibiotics: Past and Present 664\u003c\/p\u003e \u003cp\u003e24.3 Aminoglycosides as RNA Binders 666\u003c\/p\u003e \u003cp\u003e24.4 Identifying RNA Targets and Developing Binding Assays 670\u003c\/p\u003e \u003cp\u003e24.5 Dimeric Aminoglycosides 673\u003c\/p\u003e \u003cp\u003e24.6 Aminoglycoside-Intercalator Conjugates 675\u003c\/p\u003e \u003cp\u003e24.7 Guanidinoglycosides 677\u003c\/p\u003e \u003cp\u003e24.8 Summary and Outlook 679\u003c\/p\u003e \u003cp\u003e24.9 Acknowledgements 680\u003c\/p\u003e \u003cp\u003e24.10 References 680\u003c\/p\u003e \u003cp\u003e\u003cb\u003e25 Glycosylated Natural Products \u003c\/b\u003e\u003cb\u003e685\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eJon S. Thorson and Thomas Vogt\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e25.1 Introduction 685\u003c\/p\u003e \u003cp\u003e25.2 A Summary of Bioactive Glycosylated Secondary Metabolites 686\u003c\/p\u003e \u003cp\u003e25.3 Conclusions 707\u003c\/p\u003e \u003cp\u003e25.4 References 707\u003c\/p\u003e \u003cp\u003e\u003cb\u003e26 Novel Enzymatic Mechanisms in the Biosynthesis of Unusual Sugars \u003c\/b\u003e\u003cb\u003e713\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eAlexander Wong, Xuemei He, and Hung-Wen Liu\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e26.1 Introduction 713\u003c\/p\u003e \u003cp\u003e26.2 Biosynthesis of Deoxysugars 714\u003c\/p\u003e \u003cp\u003e26.3 Biosynthesis of Aminosugars 725\u003c\/p\u003e \u003cp\u003e26.4 Biosynthesis of Branched-Chain Sugars 730\u003c\/p\u003e \u003cp\u003e26.5 Epimerization Reactions 734\u003c\/p\u003e \u003cp\u003e26.6 Rearrangement of Hexose Skeletons: UDP-Galactopyranose Mutase-Catalyzed Biosynthesis of Galactofuranose 738\u003c\/p\u003e \u003cp\u003e26.7 Summary 740\u003c\/p\u003e \u003cp\u003e26.8 Acknowledgements 741\u003c\/p\u003e \u003cp\u003e26.9 References 741\u003c\/p\u003e \u003cp\u003e\u003cb\u003e27 Neoglycolipids: Identification of Functional Carbohydrate Epitopes \u003c\/b\u003e\u003cb\u003e747\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eTen Feizi, Alexander M. Lawson, and Wengang Chai\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e27.1 Rationale for Developing Neoglycolipids as Oligosaccharide Probes 747\u003c\/p\u003e \u003cp\u003e27.2 The First and Second Generation Neoglycolipids 749\u003c\/p\u003e \u003cp\u003e27.3 Mass Spectrometry of Neoglycolipids 750\u003c\/p\u003e \u003cp\u003e27.4 Scope of the Neoglycolipid Technology 752\u003c\/p\u003e \u003cp\u003e27.5 Oligosaccharide Microarrays 755\u003c\/p\u003e \u003cp\u003e27.6 Summary and Perspectives 757\u003c\/p\u003e \u003cp\u003e27.7 Acknowledgement 757\u003c\/p\u003e \u003cp\u003e27.8 References 757\u003c\/p\u003e \u003cp\u003e\u003cb\u003e28 A Preamble to Aglycone Reconstruction for Membrane-Presented Glycolipid Mimics \u003c\/b\u003e\u003cb\u003e761\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eMurugesapillai Mylvaganam and Clifford A. Lingwood\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e28.1 Introduction 761\u003c\/p\u003e \u003cp\u003e28.2 The Role of Ceramide Subtype Composition 762\u003c\/p\u003e \u003cp\u003e28.3 Effects of Ceramide Subtype Composition in the Binding of Gb\u003csub\u003e3\u003c\/sub\u003eCer to Verotoxins 764\u003c\/p\u003e \u003cp\u003e28.4 Hypothesis Regarding Lipid Replacement Structural Motifs (LRSMs) 766\u003c\/p\u003e \u003cp\u003e28.5 Effect of Replacement of GSL Fatty Acyl Chains with Rigid, Non-Planar Hydrophobic Groups 768\u003c\/p\u003e \u003cp\u003e28.6 Ada-Gb\u003csub\u003e3\u003c\/sub\u003eCer, a Functional Mimic of Membrane Presented Gb\u003csub\u003e3\u003c\/sub\u003eCer for VT Binding 769\u003c\/p\u003e \u003cp\u003e28.7 Ceramide Subtype-Dependent Binding of Heat Shock Protein Hsp70 to Sulfogalactosyl Ceramide 772\u003c\/p\u003e \u003cp\u003e28.8 Adamantyl-Acyl Ceramide is a Functional Replacement for a Ceramide-Cholesterol Composition: A Study with HIV Coat Protein gp120 775\u003c\/p\u003e \u003cp\u003e28.9 Acknowledgement 777\u003c\/p\u003e \u003cp\u003e28.10 References 777\u003c\/p\u003e \u003cp\u003e\u003cb\u003e29 Small Molecule Inhibitors of the Sulfotransferases \u003c\/b\u003e\u003cb\u003e781\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eDawn E. Verdugo, Lars C. Pedersen, and Carolyn R. Bertozzi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e29.1 Introduction: Sulfotransferases and the Biology of Sulfation 781\u003c\/p\u003e \u003cp\u003e29.2 EST as a Model ST for Inhibitor Design 783\u003c\/p\u003e \u003cp\u003e29.3 Inhibition of Representative Golgi-Resident Sulfotransferases: GST-2, GST-3, and TPST-2 792\u003c\/p\u003e \u003cp\u003e29.4 Assays for High-Throughput Screening of STs 794\u003c\/p\u003e \u003cp\u003e29.5 New Directions in Inhibitor Discovery 796\u003c\/p\u003e \u003cp\u003e29.6 Conclusions 796\u003c\/p\u003e \u003cp\u003e29.7 Acknowledgements 796\u003c\/p\u003e \u003cp\u003e29.8 References 797\u003c\/p\u003e \u003cp\u003e\u003cb\u003e30 Carbohydrate-Based Treatment of Cancer Metastasis \u003c\/b\u003e\u003cb\u003e803\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eReiji Kannagi\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e30.1 Implication of Carbohydrate Determinants in Cancer Metastasis 803\u003c\/p\u003e \u003cp\u003e30.2 Tumor Angiogenesis and Cancer-Endothelial Interaction 808\u003c\/p\u003e \u003cp\u003e30.3 Use of Monoclonal Antibodies for Inhibition of Cancer Cell-Endothelial Interaction 809\u003c\/p\u003e \u003cp\u003e30.4 Inhibitors of Selectin-Mediated Cell Adhesion 812\u003c\/p\u003e \u003cp\u003e30.5 Regulation of Selectin Expression on Endothelial Cells 814\u003c\/p\u003e \u003cp\u003e30.6 Enhanced Expression of Sialyl Lex and Sialyl Lea in Malignant Cells and its Modulation 816\u003c\/p\u003e \u003cp\u003e30.7 References 824\u003c\/p\u003e \u003cp\u003e\u003cb\u003e31 \u003ci\u003eN\u003c\/i\u003e-Acetylneuraminic Acid Derivatives and Mimetics as Anti-Influenza Agents \u003c\/b\u003e\u003cb\u003e831\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eRobin Thomson and Mark von Itzstein\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e31.1 Introduction 831\u003c\/p\u003e \u003cp\u003e31.2 Structure-Based Design of Inhibitors of Influenza Virus Sialidase 836\u003c\/p\u003e \u003cp\u003e31.3 Structure\/Activity Relationship Studies of \u003ci\u003eN\u003c\/i\u003e-Acetylneuraminic Acid-Based Influenza Virus Sialidase Inhibitors 840\u003c\/p\u003e \u003cp\u003e31.4 Concluding Remarks 856\u003c\/p\u003e \u003cp\u003e31.5 Acknowledgements 856\u003c\/p\u003e \u003cp\u003e31.6 References 857\u003c\/p\u003e \u003cp\u003e\u003cb\u003e32 Modified and Modifying Sugars as a New Tool for the Development of Therapeutic Agents – The Biochemically Engineered \u003ci\u003eN\u003c\/i\u003e-Acyl Side Chain of Sialic Acid: Biological Implications and Possible Uses in Medicine \u003c\/b\u003e\u003cb\u003e863\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eRüdiger Horstkorte, Oliver T. Keppler, and Werner Reutter\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e32.1 Introduction 863\u003c\/p\u003e \u003cp\u003e32.2 \u003ci\u003eN\u003c\/i\u003e-Acyl Side Chain-Modified Precursors of Sialic Acid 865\u003c\/p\u003e \u003cp\u003e32.3 Outlook 871\u003c\/p\u003e \u003cp\u003e32.4 Acknowledgements 872\u003c\/p\u003e \u003cp\u003e32.5 Abbreviations 872\u003c\/p\u003e \u003cp\u003e32.6 References 872\u003c\/p\u003e \u003cp\u003e\u003cb\u003e33 Modified and Modifying Sugars as a New Tool for the Development of Therapeutic Agents – Glycosidated Phospholipids as a New Type of Antiproliferative Agents \u003c\/b\u003e\u003cb\u003e875\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eKerstin Danker, Annette Fischer, and Werner Reutter\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e33.1 Introduction 875\u003c\/p\u003e \u003cp\u003e33.2 Structures of Synthetic Glycosidated Phospholipid Analogues 876\u003c\/p\u003e \u003cp\u003e33.3 Antiproliferative Effect and Cytotoxicity of Glycosidated Phospholipid Analogues in Cell Culture Systems 876\u003c\/p\u003e \u003cp\u003e33.4 Effect of Glycosidated Phospholipid Analogues on Cell Matrix Adhesion 878\u003c\/p\u003e \u003cp\u003e33.5 Mechanisms of Action 879\u003c\/p\u003e \u003cp\u003e33.6 Outlook and New Developments 880\u003c\/p\u003e \u003cp\u003e33.7 Acknowledgements 881\u003c\/p\u003e \u003cp\u003e33.8 References 881\u003c\/p\u003e \u003cp\u003e\u003cb\u003e34 Glycoside Primers and Inhibitors of Glycosylation \u003c\/b\u003e\u003cb\u003e883\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eJillian R. Brown, Mark M. Fuster, and Jeffrey D. Esko\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e34.1 Introduction 883\u003c\/p\u003e \u003cp\u003e34.2 Glycoside-Based Substrates 883\u003c\/p\u003e \u003cp\u003e34.3 Glycoside Primers – Xylosides 884\u003c\/p\u003e \u003cp\u003e34.4 Other Types of Primers 885\u003c\/p\u003e \u003cp\u003e34.5 Glycosides as Metabolic Decoys 888\u003c\/p\u003e \u003cp\u003e34.6 Analogues 890\u003c\/p\u003e \u003cp\u003e34.7 References 892\u003c\/p\u003e \u003cp\u003e\u003cb\u003e35 Carbohydrate-Based Drug Discovery in the Battle Against Bacterial Infections: New Opportunities Arising from Programmable One-Pot Oligosaccharide Synthesis \u003c\/b\u003e\u003cb\u003e899\u003cbr\u003e\u003c\/b\u003e\u003ci\u003eThomas K. Ritter and Chi-Huey Wong\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e35.1 Introduction 899\u003c\/p\u003e \u003cp\u003e35.2 Cell-Surface Carbohydrates 900\u003c\/p\u003e \u003cp\u003e35.3 Peptidoglycan 904\u003c\/p\u003e \u003cp\u003e35.4 Macrolide Antibiotics 913\u003c\/p\u003e \u003cp\u003e35.5 Aminoglycosides 917\u003c\/p\u003e \u003cp\u003e35.6 Programmable One-Pot Oligosaccharide Synthesis 922\u003c\/p\u003e \u003cp\u003e35.7 Summary 927\u003c\/p\u003e \u003cp\u003e35.8 References 928\u003c\/p\u003e \u003cp\u003eSubject Index 933\u003c\/p\u003e","brand":"Wiley-VCH Verlag GmbH","offers":[{"title":"Default Title","offer_id":51044078387543,"sku":"9783527306329","price":498.75,"currency_code":"GBP","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9783527306329.jpg?v=1750960476","url":"https:\/\/bookcurl.com\/products\/carbohydrate-based-drug-discovery-2-volume-set-9783527306329","provider":"Book Curl","version":"1.0","type":"link"}